Determination of Hemin-Binding Characteristics of Proteins by a Combinatorial Peptide Library Approach

ChemBioChem ◽  
2011 ◽  
Vol 12 (18) ◽  
pp. 2846-2855 ◽  
Author(s):  
Toni Kühl ◽  
Nirakar Sahoo ◽  
Melanie Nikolajski ◽  
Bernhard Schlott ◽  
Stefan H. Heinemann ◽  
...  
Keyword(s):  
Peptide Library ◽  
Binding Characteristics ◽  
Combinatorial Peptide Library ◽  
Peptide Library Approach

Determination of Substrate Specificity for Peptide Deformylase through the Screening of a Combinatorial Peptide Library†

Biochemistry ◽  
1999 ◽  
Vol 38 (2) ◽  
pp. 643-650 ◽  
Author(s):  
Yun-Jin Hu ◽  
Yaoming Wei ◽  
Ying Zhou ◽  
P. T. Ravi Rajagopalan ◽  
Dehua Pei
Keyword(s):  
Substrate Specificity ◽  
Peptide Library ◽  
Peptide Deformylase ◽  
Combinatorial Peptide Library

The Substrate Specificity of a Recombinant Cysteine Protease fromLeishmania mexicana: Application of a Combinatorial Peptide Library Approach

ChemBioChem ◽  
2000 ◽  
Vol 1 (2) ◽  
pp. 115-122 ◽  
Author(s):  
Phaedria M. St. Hilaire ◽  
Lira C. Alves ◽  
Sanya J. Sanderson ◽  
Jeremy C. Mottram ◽  
Maria A. Juliano ◽  
...  
Keyword(s):  
Substrate Specificity ◽  
Cysteine Protease ◽  
Peptide Library ◽  
Combinatorial Peptide Library ◽  
Peptide Library Approach

scholarly journals Determination of substrate motifs for human Chk1 and hCds1/Chk2 by the oriented peptide library approach.

2002 ◽  
Vol 277 (38) ◽  
pp. 35776-35777
Author(s):  
Ted O'Neill ◽  
Lauren Giarratani ◽  
Ping Chen ◽  
Lakshmanan Iyer ◽  
Chang-Hun Lee ◽  
...  
Keyword(s):  
Peptide Library ◽  
Peptide Library Approach

scholarly journals Determination of Substrate Motifs for Human Chk1 and hCds1/Chk2 by the Oriented Peptide Library Approach

2002 ◽  
Vol 277 (18) ◽  
pp. 16102-16115 ◽  
Author(s):  
Ted O'Neill ◽  
Lauren Giarratani ◽  
Ping Chen ◽  
Lakshmanan Iyer ◽  
Chang-Hun Lee ◽  
...  
Keyword(s):  
Peptide Library ◽  
Peptide Library Approach

Determination of the Sequence Specificity of XIAP BIR Domains by Screening a Combinatorial Peptide Library†

Biochemistry ◽  
2006 ◽  
Vol 45 (49) ◽  
pp. 14740-14748 ◽  
Author(s):  
Michael C. Sweeney ◽  
Xianxi Wang ◽  
Junguk Park ◽  
Yusen Liu ◽  
Dehua Pei
Keyword(s):  
Peptide Library ◽  
Sequence Specificity ◽  
Combinatorial Peptide Library

Quantitative Assessment of Soluble Fibrin in Plasma by Affinity Chromatography – A Comparative Study with desAA-Fibrin, desAABB-Fibrin and Fibrinogen

1985 ◽  
Vol 54 (02) ◽  
pp. 533-538 ◽  
Author(s):  
Wilfried Thiel ◽  
Ulrich Delvos ◽  
Gert Müller-Berghaus
Keyword(s):  
Affinity Chromatography ◽  
Calcium Ions ◽  
Quantitative Assessment ◽  
Fluid Phase ◽  
Soluble Fibrin ◽  
Binding Characteristics ◽  
Different Temperatures ◽  
Immobilized Proteins ◽  
Sepharose 4B

SummaryA quantitative determination of soluble fibrin in plasma was carried out by affinity chromatography. For this purpose, desAA-fibrin and fibrinogen immobilized on Sepharose 4B were used at the stationary side whereas batroxobin-induced 125I-desAA-fibrin or thrombin-induced 125I-desAABB-fibrin mixed with plasma containing 131I-fibrinogen represented the fluid phase. The binding characteristics of these mixtures to the immobilized proteins were compared at 20° C and 37° C. Complete binding of both types of fibrin to the immobilized desAA-fibrin was always seen at 20° C as well as at 37° C. However, binding of soluble fibrin was accompanied by substantial binding of fibrinogen that was more pronounced at 20° C. Striking differences depending on the temperature at which the affinity chromatography was carried out, were documented for the fibrinogen-fibrin interaction. At 20° C more than 90% of the applied desAA-fibrin was bound to the immobilized fibrinogen whereas at 37° C only a mean of 17% were retained at the fibrinogen-Sepharose column. An opposite finding with regard to the tested temperature was made with the desAABB-fibrin. Nearly complete binding to insolubilized fibrinogen was found at 37° C (95%) but only 58% of the desAABB-fibrin were bound at 20° C. The binding patterns did not change when the experiments were performed in the presence of calcium ions. The opposite behaviour of the two types of soluble fibrin to immobilized fibrinogen at the different temperatures, together with the substantial binding of fibrinogen in the presence of soluble fibrin to insolubilized fibrin in every setting tested, devaluates affinity chromatography as a tool in the quantitative assessment of soluble fibrin in patients’ plasma.

Rapid Identification of Substrates for Novel Proteases Using a Combinatorial Peptide Library

2000 ◽  
Vol 2 (5) ◽  
pp. 461-466 ◽  
Author(s):  
Gérard Rossé ◽  
Erich Kueng ◽  
Malcolm G. P. Page ◽  
Vesna Schauer-Vukasinovic ◽  
Thomas Giller ◽  
...  
Keyword(s):  
Rapid Identification ◽  
Peptide Library ◽  
Combinatorial Peptide Library

scholarly journals Rapid Determination of Substrate Specificity ofClostridium histolyticumβ-Collagenase Using an Immobilized Peptide Library

2001 ◽  
Vol 277 (10) ◽  
pp. 8366-8371 ◽  
Author(s):  
Yongbo Hu ◽  
Erin Webb ◽  
Jasbir Singh ◽  
Barry A. Morgan ◽  
James A. Gainor ◽  
...  
Keyword(s):  
Substrate Specificity ◽  
Rapid Determination ◽  
Peptide Library ◽  
Immobilized Peptide

scholarly journals Enhanced protein synthesis and secretion using a rational signal-peptide library approach as a tailored tool

2011 ◽  
Vol 5 (S8) ◽  
Author(s):  
Beate Stern ◽  
Asta Optun ◽  
Melanie Liesenfeld ◽  
Christine Gey ◽  
Markus Gräfe ◽  
...  
Keyword(s):  
Protein Synthesis ◽  
Signal Peptide ◽  
Peptide Library ◽  
Peptide Library Approach
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